Mechanistic and structural studies of KDM-catalysed demethylation of histone 1 isotype 4 at lysine 26.
FEBS Lett
; 592(19): 3264-3273, 2018 10.
Article
em En
| MEDLINE
| ID: mdl-30156264
ABSTRACT
N-Methylation of lysyl residues is widely observed on histone proteins. Using isolated enzymes, we report mechanistic and structural studies on histone lysine demethylase (KDM)-catalysed demethylation of Nε -methylated lysine 26 on histone 1 isotype 4 (H1.4). The results reveal that methylated H1.4K26 is a substrate for all members of the KDM4 subfamily and that KDM4A-catalysed demethylation of H1.4K26me3 peptide is similarly efficient to that of H3K9me3. Crystallographic studies of an H1.4K26me3KDM4A complex reveal a conserved binding geometry to that of H3K9me3. In the light of the high activity of the KDM4s on this mark, our results suggest JmjC KDM-catalysed demethylation of H1.4K26 may be as prevalent as demethylation on the H3 tail and warrants further investigation in cells.
Palavras-chave
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Histonas
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Histona Desmetilases com o Domínio Jumonji
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Desmetilação
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Lisina
Limite:
Humans
Idioma:
En
Revista:
FEBS Lett
Ano de publicação:
2018
Tipo de documento:
Article